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Literature summary extracted from
- Cloning and expression of Bacillus phytase gene (phy) in Escherichia coli and recovery of active enzyme from the inclusion bodies (2008), J. Appl. Microbiol., 105, 1128-1137.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | expression in Escherichia coli | Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | expressed in Escherichia coli | Bacillus sp. (in: Bacteria) |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | EDTA | - |
Bacillus sp. (in: Bacteria) |  |
| 3.1.3.26 | EDTA | - |
Bacillus sp. (in: Bacteria) | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.8 | 0.39 | - |
myo-inositol hexakisphosphate | 37°C, pH 7.0 | Bacillus sp. (in: Bacteria) | |
| 3.1.3.26 | 0.392 | - |
myo-inositol hexakisphosphate | - |
Bacillus sp. (in: Bacteria) | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | Ca2+ | required both for refolding and activity | Bacillus sp. (in: Bacteria) | |
| 3.1.3.8 | additional information | enzyme refolded in presence of Cu2+, Fe2+, Mg2+, Co2+, Zn2+ or Mn2+, fails to show any enzyme activity even in the presence of Ca2+ in the reaction mix | Bacillus sp. (in: Bacteria) | |
| 3.1.3.26 | Ca2+ | is found essential for both refolding and activity of the enzyme | Bacillus sp. (in: Bacteria) | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 40000 | - |
x * 40000, SDS-PAGE | Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 40000 | - |
SDS-PAGE | Bacillus sp. (in: Bacteria) |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Bacillus sp. (in: Bacteria) | A5A5J1 | - |
- |
| 3.1.3.8 | Bacillus sp. (in: Bacteria) DECSR1 | A5A5J1 | - |
- |
| 3.1.3.26 | Bacillus sp. (in: Bacteria) | A5A5J1 | The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate; the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | recombinant protein, from inclusion bodies | Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | the transformant with phy is cultivated in the bioreactor. The cell mass obtained after 9 h of cultivation is 26.81 g wet weight per litre yielding 4289 U (micromol/min) enzyme activity when compared to 1.978 g wet weight per litre mass producing 256 U (micromol/min) activity in shake-flask cultures | Bacillus sp. (in: Bacteria) |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | Ca2+ is required for refolding. Enzyme refolded in the presence of one of the divalent cations, Cu2+, Fe2+, Mg2+, Co2+, Zn2+ or Mn2+, fails to show any enzyme activity even in the presence of Ca2+ in the reaction mix | Bacillus sp. (in: Bacteria) |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 16 | - |
37°C, pH 7.0 | Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 16 | - |
- |
Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Bacillus sp. (in: Bacteria) | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Bacillus sp. (in: Bacteria) DECSR1 | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Bacillus sp. (in: Bacteria) | ? + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | Bacillus sp. (in: Bacteria) DECSR1 | ? + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 40000, SDS-PAGE | Bacillus sp. (in: Bacteria) |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.26 | Phy | - |
Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | phytase | - |
Bacillus sp. (in: Bacteria) |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 55 | - |
- |
Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 55 | - |
- |
Bacillus sp. (in: Bacteria) |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 25 | 70 | - |
Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 25 | 70 | - |
Bacillus sp. (in: Bacteria) |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.26 | additional information | - |
the enzyme upon denaturation for 10 min at 75, 85 and 95°C, followed by 1 h renaturation at the room temperature (28°C) in the presence of 5 mmol/l Ca2+, restores 86%, 54%, and 37% activity | Bacillus sp. (in: Bacteria) |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 7 | - |
- |
Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 7 | - |
- |
Bacillus sp. (in: Bacteria) |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 5 | 8 | - |
Bacillus sp. (in: Bacteria) |
| 3.1.3.26 | 5 | 8 | - |
Bacillus sp. (in: Bacteria) |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.26 | additional information | - |
the enzyme shows a recovery of 45% activity when it is preincubated at pH 3.0 and 37°C for 6 h prior to phytase assay | Bacillus sp. (in: Bacteria) |
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